Structural and functional studies of conserved nucleotide-binding protein LptB in lipopolysaccharide transport

Biochemical and Biophysical Research Communications

Volumn 452, Issue 3, 2014, Pages 443-449

  Wang, Zhongshan ^a,b,c   Xiang, Quanju ^b,c,d   Zhu, Xiaofeng ^b   Dong, Haohao ^c   He, Chuan ^e   Wang, Haiyan ^b   Zhang, Yizheng ^b   Wang, Wenjian ^f   Dong, Changjiang ^a  

^a UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^b SICHUAN UNIVERSITY   (China)

^c UNIVERSITY OF ST ANDREWS   (United Kingdom)

^d SICHUAN AGRICULTURAL UNIVERSITY   (China)

^e Wuhan Technical College of Communications   (China)

^f SUN YAT SEN UNIVERSITY   (China)

Author keywords

Crystal structure and function; Gram negative bacteria; Lipopolysaccharide transport protein; LptB; Nucleotide binding protein

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALANINE; LIPOPOLYSACCHARIDE; MAGNESIUM; NUCLEOTIDE BINDING PROTEIN; PROTEIN LPTB; UNCLASSIFIED DRUG; ABC TRANSPORTER; ESCHERICHIA COLI PROTEIN; LPTB PROTEIN, E COLI; PROTEIN BINDING; RECOMBINANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; NONHUMAN; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN STRUCTURE; TRANSMISSION ELECTRON MICROSCOPY; AMINO ACID SEQUENCE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; GENE EXPRESSION; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROMOTER REGION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTEIN TRANSPORT;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ATP-BINDING CASSETTE TRANSPORTERS; BINDING SITES; CONSERVED SEQUENCE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION; GENE EXPRESSION REGULATION, BACTERIAL; LIPOPOLYSACCHARIDES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROMOTER REGIONS, GENETIC; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; RECOMBINANT PROTEINS;

EID: 84907504111     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.08.094     Document Type: Article

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